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Conserved domains on  [gi|7106335|ref|NP_034793|]
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keratin, type I cytoskeletal 17 [Mus musculus]

Protein Classification

intermediate filament family protein( domain architecture ID 11981676)

intermediate filament (IF) family protein is a primordial component of the cytoskeleton and the nuclear envelope; such as type I keratins

CATH:  1.20.5.170
Gene Ontology:  GO:0005882
PubMed:  2183847|12596228|28101862

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
84-394 2.99e-146

Intermediate filament protein;


:

Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 418.55  E-value: 2.99e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106335     84 EKATMQNLNDRLASYLDKVRALEEANTELEVKIRDWYQKQAPGPARDYSAYYHTIEDLKNKILVATVDNASILLQIDNAR 163
Cdd:pfam00038   2 EKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNLR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106335    164 LAADDFRTKFETEQALRMSVEADINGLRRVLDELTLARADLEMQIENLKEELAYLKKNHEEEMNALRGQVG-GEINVEMD 242
Cdd:pfam00038  82 LAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSdTQVNVEMD 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106335    243 AAPGVDLSRILSEMRDQYEKMAEKNRKDAEDWFFSKTEELNREVATNSELVQSGKSEISELRRTMQALEIELQSQLSMKA 322
Cdd:pfam00038 162 AARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQKA 241

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 7106335    323 SLEGSLAETENRYCVQLSQIQGLIGSVEEQLAQLRCEMEQQNQEYKILLDVKTRLEQEIATYRRLLEGEDAH 394
Cdd:pfam00038 242 SLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
84-394 2.99e-146

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 418.55  E-value: 2.99e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106335     84 EKATMQNLNDRLASYLDKVRALEEANTELEVKIRDWYQKQAPGPARDYSAYYHTIEDLKNKILVATVDNASILLQIDNAR 163
Cdd:pfam00038   2 EKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNLR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106335    164 LAADDFRTKFETEQALRMSVEADINGLRRVLDELTLARADLEMQIENLKEELAYLKKNHEEEMNALRGQVG-GEINVEMD 242
Cdd:pfam00038  82 LAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSdTQVNVEMD 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106335    243 AAPGVDLSRILSEMRDQYEKMAEKNRKDAEDWFFSKTEELNREVATNSELVQSGKSEISELRRTMQALEIELQSQLSMKA 322
Cdd:pfam00038 162 AARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQKA 241

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 7106335    323 SLEGSLAETENRYCVQLSQIQGLIGSVEEQLAQLRCEMEQQNQEYKILLDVKTRLEQEIATYRRLLEGEDAH 394
Cdd:pfam00038 242 SLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 173-389 6.65e-09

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 58.14  E-value: 6.65e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106335     173 FETEQALRmSVEADINGLRRVLDELTLARADLEMQIENLKEELAYLKKNHEE---EMNALRGQVGG-EINVEMDAAPGVD 248
Cdd:TIGR02168  673 LERRREIE-ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEElsrQISALRKDLARlEAEVEQLEERIAQ 751

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106335     249 LSRILSEMRDQYEKMAEKNRK--DAEDWFFSKTEELNREVATNSELVQSGKSEISELRRTMQALEIELQSQLSMKASLEG 326
Cdd:TIGR02168  752 LSKELTELEAEIEELEERLEEaeEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLER 831

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 7106335     327 SLAETENRYCV---QLSQIQGLIGSVEEQLAQLRCEMEQQNQEYKILLDVKTRLEQEIATYRRLLE 389
Cdd:TIGR02168  832 RIAATERRLEDleeQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELE 897
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 174-382 4.92e-07

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 51.69  E-value: 4.92e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106335  174 ETEQALRmSVEADINGLRRVLDELTLARADLEMQIENLKEELAYLKK---NHEEEMNALRGQVGgEINVEMDAapgvdLS 250
Cdd:COG4942  24 EAEAELE-QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARrirALEQELAALEAELA-ELEKEIAE-----LR 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106335  251 RILSEMRDQYEKMAEK----NRKDAEDWFFSKTE--ELNREVATNSELVQSGKSEISELRRTMQALEIELQSQLSMKASL 324
Cdd:COG4942  97 AELEAQKEELAELLRAlyrlGRQPPLALLLSPEDflDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAEL 176

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 7106335  325 EGSLAETENrycvQLSQIQGLIGSVEEQLAQLRCEMEQQNQEYKILLDVKTRLEQEIA 382
Cdd:COG4942 177 EALLAELEE----ERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIA 230
 
Name Accession Description Interval E-value
Filament pfam00038
Intermediate filament protein;
84-394 2.99e-146

Intermediate filament protein;


Pssm-ID: 459643 [Multi-domain]  Cd Length: 313  Bit Score: 418.55  E-value: 2.99e-146
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106335     84 EKATMQNLNDRLASYLDKVRALEEANTELEVKIRDWYQKQAPGPARDYSAYYHTIEDLKNKILVATVDNASILLQIDNAR 163
Cdd:pfam00038   2 EKEQLQELNDRLASYIDKVRFLEQQNKLLETKISELRQKKGAEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNLR 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106335    164 LAADDFRTKFETEQALRMSVEADINGLRRVLDELTLARADLEMQIENLKEELAYLKKNHEEEMNALRGQVG-GEINVEMD 242
Cdd:pfam00038  82 LAAEDFRQKYEDELNLRTSAENDLVGLRKDLDEATLARVDLEAKIESLKEELAFLKKNHEEEVRELQAQVSdTQVNVEMD 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106335    243 AAPGVDLSRILSEMRDQYEKMAEKNRKDAEDWFFSKTEELNREVATNSELVQSGKSEISELRRTMQALEIELQSQLSMKA 322
Cdd:pfam00038 162 AARKLDLTSALAEIRAQYEEIAAKNREEAEEWYQSKLEELQQAAARNGDALRSAKEEITELRRTIQSLEIELQSLKKQKA 241

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 7106335    323 SLEGSLAETENRYCVQLSQIQGLIGSVEEQLAQLRCEMEQQNQEYKILLDVKTRLEQEIATYRRLLEGEDAH 394
Cdd:pfam00038 242 SLERQLAETEERYELQLADYQELISELEAELQETRQEMARQLREYQELLNVKLALDIEIATYRKLLEGEECR 313
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 173-389 6.65e-09

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 58.14  E-value: 6.65e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106335     173 FETEQALRmSVEADINGLRRVLDELTLARADLEMQIENLKEELAYLKKNHEE---EMNALRGQVGG-EINVEMDAAPGVD 248
Cdd:TIGR02168  673 LERRREIE-ELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEElsrQISALRKDLARlEAEVEQLEERIAQ 751

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106335     249 LSRILSEMRDQYEKMAEKNRK--DAEDWFFSKTEELNREVATNSELVQSGKSEISELRRTMQALEIELQSQLSMKASLEG 326
Cdd:TIGR02168  752 LSKELTELEAEIEELEERLEEaeEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLER 831

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 7106335     327 SLAETENRYCV---QLSQIQGLIGSVEEQLAQLRCEMEQQNQEYKILLDVKTRLEQEIATYRRLLE 389
Cdd:TIGR02168  832 RIAATERRLEDleeQIEELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELE 897
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 171-389 9.33e-08

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 54.68  E-value: 9.33e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106335     171 TKFETEQALRMSVEADINGLRRVLDELTLARADLEMQIENLKEELAYLKKNHE-----------------EEMNALRGQV 233
Cdd:TIGR02168  267 EKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEeleaqleeleskldelaEELAELEEKL 346

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106335     234 gGEINVEMDAapgvdLSRILSEMRDQYEKMAEKNRKDAEDWffsktEELNREVATNSELVQSGKSEISELRRTMQALEIE 313
Cdd:TIGR02168  347 -EELKEELES-----LEAELEELEAELEELESRLEELEEQL-----ETLRSKVAQLELQIASLNNEIERLEARLERLEDR 415

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 7106335     314 LQSQLSMKASLEGSLAETEnrycvqLSQIQGLIGSVEEQLAQLRCEMEQQNQEYKILLDVKTRLEQEIATYRRLLE 389
Cdd:TIGR02168  416 RERLQQEIEELLKKLEEAE------LKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELA 485
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 138-383 1.46e-07

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 53.91  E-value: 1.46e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106335     138 IEDLKNKILVATVDNASILLQIDNARLAADDFRTKFETEQALRMSVEADINGLRRVLDELTLARADLEMQIENLKEELAY 217
Cdd:TIGR02168  693 IAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEE 772

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106335     218 L---KKNHEEEMNALRGQVGG-EINVEMDAAPGVDLSRILSEMRDQY------EKMAEKNRKDAEDWFfsktEELNREVA 287
Cdd:TIGR02168  773 AeeeLAEAEAEIEELEAQIEQlKEELKALREALDELRAELTLLNEEAanlrerLESLERRIAATERRL----EDLEEQIE 848

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106335     288 TNSELVQSGKSEISELRRTMQALEIELQSQLSMKASLEGSLAETENRYCVQLSQIQgligSVEEQLAQLRCEMEQQNQEY 367
Cdd:TIGR02168  849 ELSEDIESLAAEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELR----ELESKRSELRRELEELREKL 924

                          250
                   ....*....|....*.
gi 7106335     368 KILLDVKTRLEQEIAT 383
Cdd:TIGR02168  925 AQLELRLEGLEVRIDN 940
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 174-382 4.92e-07

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 51.69  E-value: 4.92e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106335  174 ETEQALRmSVEADINGLRRVLDELTLARADLEMQIENLKEELAYLKK---NHEEEMNALRGQVGgEINVEMDAapgvdLS 250
Cdd:COG4942  24 EAEAELE-QLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARrirALEQELAALEAELA-ELEKEIAE-----LR 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106335  251 RILSEMRDQYEKMAEK----NRKDAEDWFFSKTE--ELNREVATNSELVQSGKSEISELRRTMQALEIELQSQLSMKASL 324
Cdd:COG4942  97 AELEAQKEELAELLRAlyrlGRQPPLALLLSPEDflDAVRRLQYLKYLAPARREQAEELRADLAELAALRAELEAERAEL 176

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 7106335  325 EGSLAETENrycvQLSQIQGLIGSVEEQLAQLRCEMEQQNQEYKILLDVKTRLEQEIA 382
Cdd:COG4942 177 EALLAELEE----ERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIA 230
MAD pfam05557
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ...
 201-398 8.01e-06

Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint (Mitotic arrest deficient or MAD) proteins. The mitotic spindle checkpoint monitors proper attachment of the bipolar spindle to the kinetochores of aligned sister chromatids and causes a cell cycle arrest in prometaphase when failures occur. Multiple components of the mitotic spindle checkpoint have been identified in yeast and higher eukaryotes. In S.cerevisiae, the existence of a Mad1-dependent complex containing Mad2, Mad3, Bub3 and Cdc20 has been demonstrated.


Pssm-ID: 461677 [Multi-domain]  Cd Length: 660  Bit Score: 48.20  E-value: 8.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106335    201 RADLEMQIENLKEELAYLKKNHEEEMN-ALRGQVGGEINVEMDAAPGVDLSRILSEMRDQYEKMAEKNRKDAE------- 272
Cdd:pfam05557   4 LIESKARLSQLQNEKKQMELEHKRARIeLEKKASALKRQLDRESDRNQELQKRIRLLEKREAEAEEALREQAElnrlkkk 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106335    273 --DWFFSKTEELNREVATNSELVQSGKSEISELRRTMQALEIELQSQLSMKASLEGSLAETENRY------CVQLSQIQG 344
Cdd:pfam05557  84 ylEALNKKLNEKESQLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKAseaeqlRQNLEKQQS 163

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 7106335    345 LIGSVEEQLAQLRCEMEQQNQEYKILLDVKTRLEQeIATYRRLLEGEDAHLTQY 398
Cdd:pfam05557 164 SLAEAEQRIKELEFEIQSQEQDSEIVKNSKSELAR-IPELEKELERLREHNKHL 216
GumC COG3206
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
190-389 1.85e-05

Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442439 [Multi-domain]  Cd Length: 687  Bit Score: 46.93  E-value: 1.85e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106335  190 LRRVLDELTLARADLEMQIENLKEELAylkkNHEEEMNALRGQVGGeINVEMDAApgvDLSRILSEMRDQYEKmAEKNRK 269
Cdd:COG3206 166 LELRREEARKALEFLEEQLPELRKELE----EAEAALEEFRQKNGL-VDLSEEAK---LLLQQLSELESQLAE-ARAELA 236

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106335  270 DAEDWFFSKTEELNREVATNSELVQSgkSEISELRRTMQALEIELQSQLS--------------MKASLEGSLAETENRY 335
Cdd:COG3206 237 EAEARLAALRAQLGSGPDALPELLQS--PVIQQLRAQLAELEAELAELSArytpnhpdvialraQIAALRAQLQQEAQRI 314

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 7106335  336 cvqLSQIQGLIGSVEEQLAQLRCEMEQQNQEYKILLDVK---TRLEQEIATYRRLLE 389
Cdd:COG3206 315 ---LASLEAELEALQAREASLQAQLAQLEARLAELPELEaelRRLEREVEVARELYE 368
Smc COG1196
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ...
 138-393 1.21e-04

Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 440809 [Multi-domain]  Cd Length: 983  Bit Score: 44.54  E-value: 1.21e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106335  138 IEDLKNKILVATVDNASILLQIDNARLAADDFRTKFETEQALRMSVEADI--------------NGLRRVLDELTLARAD 203
Cdd:COG1196 248 LEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELarleqdiarleerrRELEERLEELEEELAE 327

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106335  204 LEMQIENLKEELAYLKKNHEEEMNALRgqvggeinvemdaapgvDLSRILSEMRDQYEKMAEKNRKDAEDWffsktEELN 283
Cdd:COG1196 328 LEEELEELEEELEELEEELEEAEEELE-----------------EAEAELAEAEEALLEAEAELAEAEEEL-----EELA 385

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106335  284 REVATNSELVQSGKSEISELRRTMQALEIELQSQLSMKASLEGSLAETENrycvQLSQIQGLIGSVEEQLAQLRCEMEQQ 363
Cdd:COG1196 386 EELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEE----EEEEEEEALEEAAEEEAELEEEEEAL 461

                       250       260       270
                ....*....|....*....|....*....|
gi 7106335  364 NQEYKILLDVKTRLEQEIATYRRLLEGEDA 393
Cdd:COG1196 462 LELLAELLEEAALLEAALAELLEELAEAAA 491
SMC_prok_B TIGR02168
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ...
 139-353 5.15e-04

chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]


Pssm-ID: 274008 [Multi-domain]  Cd Length: 1179  Bit Score: 42.74  E-value: 5.15e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106335     139 EDLKNKILVATVDNASILLQIDNARLAADDFRTKFETEQALRMSVEADINGLRRVLDELTLARADLEMQIENLKEELAYL 218
Cdd:TIGR02168  312 ANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQLETLRSKVAQL 391

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106335     219 kknhEEEMNALRGQVggEINVEMDAAPGVDLSRILSEMRDQYEKMAEKNRKDAEDWFFSKTEELNREVATNSELVQSGKS 298
Cdd:TIGR02168  392 ----ELQIASLNNEI--ERLEARLERLEDRRERLQQEIEELLKKLEEAELKELQAELEELEEELEELQEELERLEEALEE 465

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 7106335     299 ---EISELRRTMQALEIELQSQLSMKASLEGSL--AETENRYCVQL----SQIQGLIGSVEEQL 353
Cdd:TIGR02168  466 lreELEEAEQALDAAERELAQLQARLDSLERLQenLEGFSEGVKALlknqSGLSGILGVLSELI 529
SCP-1 pfam05483
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ...
 156-417 6.35e-04

Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.


Pssm-ID: 114219 [Multi-domain]  Cd Length: 787  Bit Score: 42.02  E-value: 6.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106335    156 LLQIDNARLAADDFRTKFETEQALRMSVEADINglrrvLDELTLARADLEMQIENLKEELAYLKKNHEEEMNALRGQVGG 235
Cdd:pfam05483 159 LLKETCARSAEKTKKYEYEREETRQVYMDLNNN-----IEKMILAFEELRVQAENARLEMHFKLKEDHEKIQHLEEEYKK 233

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106335    236 EINVEMDAAPGV------------DLSRILSEMRDQYEKMAEKNRKDAEDW--FFSKTEELNREVATNSELVQSGKSEIS 301
Cdd:pfam05483 234 EINDKEKQVSLLliqitekenkmkDLTFLLEESRDKANQLEEKTKLQDENLkeLIEKKDHLTKELEDIKMSLQRSMSTQK 313

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106335    302 ELRRTMQAL---------EIELQSQLSMKASLEGSLAETENRYCV-----QLSQIQGLIGSVEEQLAQLRCEMEQQNQEY 367
Cdd:pfam05483 314 ALEEDLQIAtkticqlteEKEAQMEELNKAKAAHSFVVTEFEATTcsleeLLRTEQQRLEKNEDQLKIITMELQKKSSEL 393

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 7106335    368 KILLDVKTRLEQEIATYRRLLeGEDAHLTQYKpkepvttRQVRTIVEEVQ 417
Cdd:pfam05483 394 EEMTKFKNNKEVELEELKKIL-AEDEKLLDEK-------KQFEKIAEELK 435
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
 158-363 1.31e-03

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 40.90  E-value: 1.31e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106335  158 QIDNARLAADDFRTKFETEQALRMSVEADINGLRRVLDELTLARADLEMQIENLKEELAYLKKNHEEEMNALRGQVG--- 234
Cdd:COG4942  35 EIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAELLRaly 114

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106335  235 -----GEINVEMDAAPGVDLSRILsemrdQYEKMAEKNRKDAEDWFFSKTEELNREVATNSELVQSGKSEISELRRTMQA 309
Cdd:COG4942 115 rlgrqPPLALLLSPEDFLDAVRRL-----QYLKYLAPARREQAEELRADLAELAALRAELEAERAELEALLAELEEERAA 189

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....
gi 7106335  310 LEIELQSQLSMKASLEGSLAETENrycvQLSQIQGLIGSVEEQLAQLRCEMEQQ 363
Cdd:COG4942 190 LEALKAERQKLLARLEKELAELAA----ELAELQQEAEELEALIARLEAEAAAA 239
CCDC158 pfam15921
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ...
 83-409 1.78e-03

Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.


Pssm-ID: 464943 [Multi-domain]  Cd Length: 1112  Bit Score: 40.87  E-value: 1.78e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106335      83 GEKATMQN----LNDRLASYLDKVRALEEANTEL-------EVKIRDWYQKQAPGparDYSAYYHTiEDLKNKILVATVD 151
Cdd:pfam15921  486 AKKMTLESsertVSDLTASLQEKERAIEATNAEItklrsrvDLKLQELQHLKNEG---DHLRNVQT-ECEALKLQMAEKD 561

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106335     152 NASILL--QIDN-ARLAADDFRTKfETEQALRMSVEADINGLRRVLDELTLAR-------ADLEMQIENLKEELAYLKKN 221
Cdd:pfam15921  562 KVIEILrqQIENmTQLVGQHGRTA-GAMQVEKAQLEKEINDRRLELQEFKILKdkkdakiRELEARVSDLELEKVKLVNA 640

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106335     222 HEEEMNALRgqvggEINVEMDAAPG-VDLSRI-LSEMRDQYEKMAEKnrkdaedwFFSKTEELnrEVATNSELVQ--SGK 297
Cdd:pfam15921  641 GSERLRAVK-----DIKQERDQLLNeVKTSRNeLNSLSEDYEVLKRN--------FRNKSEEM--ETTTNKLKMQlkSAQ 705

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106335     298 SEISELRRTMQALEIELQSQLSMKASLEGslaetenrycvQLSQIQGLIGSVEEQLAQLRCEMEQQNQEYKILLDVKTRL 377
Cdd:pfam15921  706 SELEQTRNTLKSMEGSDGHAMKVAMGMQK-----------QITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKL 774

                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 7106335     378 EQE---IATYRRLLEGEDAHL--TQYKPKEPVTTRQV 409
Cdd:pfam15921  775 SQElstVATEKNKMAGELEVLrsQERRLKEKVANMEV 811
CwlO1 COG3883
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ...
 182-366 3.54e-03

Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];


Pssm-ID: 443091 [Multi-domain]  Cd Length: 379  Bit Score: 39.43  E-value: 3.54e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106335  182 SVEADINGLRRVLDELTLARADLEMQIENLKEELAYLKKN---HEEEMNALRGQVGGEINVE-MDAAPGVDLSRILSEmr 257
Cdd:COG3883  34 AAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEiaeAEAEIEERREELGERARALyRSGGSVSYLDVLLGS-- 111

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 7106335  258 dqyekmaeknrKDAEDwFFSKTEELNREVATNSELVQSGKSEISELRRTMQALEIELQSQLSMKASLEGSLAETENrycv 337
Cdd:COG3883 112 -----------ESFSD-FLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEA---- 175

                       170       180
                ....*....|....*....|....*....
gi 7106335  338 QLSQIQGLIGSVEEQLAQLRCEMEQQNQE 366
Cdd:COG3883 176 QQAEQEALLAQLSAEEAAAEAQLAELEAE 204
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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